EC Number   |
General Information |
Reference |
|---|
  4.2.1.129 | evolution |
enzyme distribution in the different taxa, overview |
726715 |
| 4.2.1.129 | metabolism |
the enzyme converts squalene to hopanol, EC 4.2.1.129 as well as to tetrahymanol, EC 4.2.1.123, but not to hopene, EC 5.4.99.17, pathway overview |
726715 |
| 4.2.1.129 | metabolism |
the enzyme converts squalene to hopanol, EC 4.2.1.129, and to hopene, EC 5.4.99.17, but not to tetrahymanol, EC 4.2.1.123, pathway overview |
726715 |
| 4.2.1.129 | metabolism |
the enzyme converts squalene to hopanol, EC 4.2.1.129, but not to tetrahymanol, EC 4.2.1.123, and not to hopene, EC 5.4.99.17, pathway overview |
726715 |
| 4.2.1.129 | metabolism |
the enzyme converts squalene to hopanol, EC 4.2.1.129, but not to tetrahymanol, EC 4.2.1.123, pathway overview |
726715 |
| 4.2.1.129 | metabolism |
the enzyme converts squalene to hopanol, pathway overview |
726715 |
| 4.2.1.129 | metabolism |
the enzyme converts squalene to tetrahymanol, EC 4.2.1.123, to hopene, EC 5.4.99.17, and to hopanol, EC 4.2.1.129, pathway overview |
726715 |
| 4.2.1.129 | more |
structure-function relationships of SHCs, active site structure, overview |
726715 |
| 4.2.1.129 | more |
structure-function relationships of SHCs, active site structure, overview. A protruding part in the center of the nonpolar region contains a lipophilic channel and directs the substrate to the active-site cavity inside the protein. The channel and cavity are separated by a narrow constriction buildup of four amino acids, D376, F166, C435, and F434, that appear to block access to the active site. Residues C435 and F434 are part of a loop that seems to be flexible enough to permit passage of the substrate and the product |
726715 |
